OCA1_YEAST
ID OCA1_YEAST Reviewed; 238 AA.
AC P50946; D6W180; Q45U02;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE EC=3.1.3.48;
DE AltName: Full=Oxidant-induced cell-cycle arrest protein 1;
GN Name=OCA1; OrderedLocusNames=YNL099C; ORFNames=N2194;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-66.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701612;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT frames.";
RL Yeast 12:403-409(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP DOMAIN.
RX PubMed=9757831; DOI=10.1016/s0968-0004(98)01241-9;
RA Wishart M.J., Dixon J.E.;
RT "Gathering STYX: phosphatase-like form predicts functions for unique
RT protein-interaction domains.";
RL Trends Biochem. Sci. 23:301-306(1998).
RN [6]
RP FUNCTION.
RX PubMed=11408586; DOI=10.1091/mbc.12.6.1801;
RA Alic N., Higgins V.J., Dawes I.W.;
RT "Identification of a Saccharomyces cerevisiae gene that is required for G1
RT arrest in response to the lipid oxidation product linoleic acid
RT hydroperoxide.";
RL Mol. Biol. Cell 12:1801-1810(2001).
RN [7]
RP FUNCTION.
RX PubMed=12912987; DOI=10.1074/jbc.m307760200;
RA Alic N., Higgins V.J., Pichova A., Breitenbach M., Dawes I.W.;
RT "Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:41849-41855(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP INTERACTION WITH OCA2; OCA4; OCA5 AND SIW14.
RX PubMed=16429126; DOI=10.1038/nature04532;
RA Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
RA Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
RA Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.-M.,
RA Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A.,
RA Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B.,
RA Bork P., Russell R.B., Superti-Furga G.;
RT "Proteome survey reveals modularity of the yeast cell machinery.";
RL Nature 440:631-636(2006).
RN [11]
RP FUNCTION.
RX PubMed=18205808; DOI=10.1111/j.1567-1364.2007.00349.x;
RA Fong C.S., Temple M.D., Alic N., Chiu J., Durchdewald M., Thorpe G.W.,
RA Higgins V.J., Dawes I.W.;
RT "Oxidant-induced cell-cycle delay in Saccharomyces cerevisiae: the
RT involvement of the SWI6 transcription factor.";
RL FEMS Yeast Res. 8:386-399(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Putative tyrosine-protein phosphatase required for protection
CC against superoxide stress. Involved in cell-cycle delay in response to
CC linoleic acid hydroperoxide (LoaOOH). {ECO:0000269|PubMed:11408586,
CC ECO:0000269|PubMed:12912987, ECO:0000269|PubMed:18205808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- INTERACTION:
CC P50946; P53949: OCA2; NbExp=5; IntAct=EBI-28814, EBI-28725;
CC P50946; P53965: SIW14; NbExp=4; IntAct=EBI-28814, EBI-28668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; DQ115393; AAZ22508.1; -; Genomic_DNA.
DR EMBL; Z50161; CAA90527.1; -; Genomic_DNA.
DR EMBL; Z71375; CAA95975.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10446.1; -; Genomic_DNA.
DR PIR; S58253; S58253.
DR RefSeq; NP_014300.3; NM_001182937.3.
DR AlphaFoldDB; P50946; -.
DR SMR; P50946; -.
DR BioGRID; 35724; 263.
DR DIP; DIP-1991N; -.
DR IntAct; P50946; 5.
DR MINT; P50946; -.
DR STRING; 4932.YNL099C; -.
DR iPTMnet; P50946; -.
DR MaxQB; P50946; -.
DR PaxDb; P50946; -.
DR PRIDE; P50946; -.
DR EnsemblFungi; YNL099C_mRNA; YNL099C; YNL099C.
DR GeneID; 855624; -.
DR KEGG; sce:YNL099C; -.
DR SGD; S000005043; OCA1.
DR VEuPathDB; FungiDB:YNL099C; -.
DR eggNOG; KOG1572; Eukaryota.
DR GeneTree; ENSGT00940000176301; -.
DR HOGENOM; CLU_047845_2_0_1; -.
DR InParanoid; P50946; -.
DR OMA; NAWDPIT; -.
DR BioCyc; YEAST:G3O-33127-MON; -.
DR PRO; PR:P50946; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P50946; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR004861; Siw14-like.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF03162; Y_phosphatase2; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..238
FT /note="Putative tyrosine-protein phosphatase OCA1"
FT /id="PRO_0000203439"
FT DOMAIN 72..230
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 66
FT /note="R -> C (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
SQ SEQUENCE 238 AA; 27205 MW; 114DD87CBA2FAEBF CRC64;
MTSKVGEYED VPEDESRLTE ENVSVPEEEV EDEDEEEDDD DDHIYINEET ESGREKVLVS
HAPQERIVPP LNFCPVERYL YRSGQPSPVN FPFLLNLKLK TIIWLSNEEP QDTLLEFCDT
HRINLQFAAI NPDAGEDDNP WDGLTEHSII NVLQTIVTQE NYPLLVCCGM GRHRTGTVIG
CLRRIMGWNL ASVSEEYRRF TGSRGGRILV ELLIEAFDTN LVKIDKNKAP SWLLTALE
